The identification of a conserved binding motif within human papillomavirus type 16 E6 binding peptides, E6AP and E6BP.
A 16-mer peptide library was screened using the yeast two-hybrid system to identify peptides which specifically interact with the human papillomavirus type 16 (HPV-16) E6 protein. Four different peptides were identified, three of which contained an E-L-L/V-G motif. A fifth E6 binding peptide, derived from the putative tumour suppressor protein tuberin, was identified during a two-hybrid screen of a HeLa cDNA expression library. This peptide contained a D-I-L-G motif. Homology to the peptides was found within the E6 binding proteins E6-AP and E6-BP. A synthetic peptide containing the ELLG motif blocked the interaction of E6 with both E6-AP and E6-BP. The data suggest that E6 interacts through a structurally similar binding domain present within a number of cellular proteins.
Elston
R C
RC
Division of Virology, National Institute for Medical Research, London, UK. relston@nimr.mrc.ac.uk
Napthine
S
S
Doorbar
J
J
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D009856:Oncogene Proteins, Viral / Q000737:chemistry / Q000378:metabolism*; D027383:Papillomaviridae / Q000502:physiology*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry; D012097:Repressor Proteins / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
C068651:E6 protein, Human papillomavirus type 16; D009856:Oncogene Proteins, Viral; D010446:Peptide Fragments; D012097:Repressor Proteins